Relationship of retrovirus polyprotein cleavages to virion maturation studied with temperature-sensitive murine leukemia virus mutants
- Creators
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Witte, Owen N.
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Baltimore, David
Abstract
Murine leukemia virus mutants ts3 (Moloney) and ts24 (Rauscher) both formed late-budding structures on the cell membrane at restrictive temperature. They both accumulated core polyproteins Pr65gag and Pr180gag-pol in cell membranes, but the envelope precursor was rapidly turned over. After shift to permissive temperature in the presence of cycloheximide, the accumulated precursors were sequentially cleaved via discrete intermediates both during the final stages of the budding process and in newly released virions to yield the finished virion core proteins and reverse transcriptase. The precursor form of reverse transcriptase was not enzymatically active and became activated partially or entirely inside released virions.
Additional Information
© 1978 American Society for Microbiology. Received for publication 3 January 1978. We thank Claire Moore for performing the electron microscopy and Michael Paskind for excellent photographic work. This research was supported by American Cancer Society grant VC-41, Public Health Service grant CA-14051 from the National Cancer Institute, and a contract from the Virus Cancer Program of the National Cancer Institute. O. N. W. is a Helen Hay Whitney Foundation postdoctoral fellow. D. B. is an American Cancer Society Professor of Microbiology.Attached Files
Published - WITjvir78.pdf
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Additional details
- PMCID
- PMC525900
- Eprint ID
- 32754
- Resolver ID
- CaltechAUTHORS:20120726-131556638
- American Cancer Society
- VC-41
- NIH
- CA-14051
- National Cancer Institute
- Helen Hay Whitney Foundation
- Created
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2012-07-30Created from EPrint's datestamp field
- Updated
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2019-10-03Created from EPrint's last_modified field